MolNFT v1 · #23220 · protein

Crystal structure of the RNase T1 variant R2

1TTO: “Crystal structure of the RNase T1 variant R2”. X-ray diffraction, 2 pockets (best druggability 0.58). MolNFT v1 #23220 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1TTO
Type: protein
Length: 312 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNase T1
EC: 3.1.27.3
UniProt: P00651
Pockets: 2 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	RNase T1 (EC 3.1.27.3)	protein	104	16% helix, 29% strand	P00651

Ligands and binding sites

TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 3 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	302	0.58	0.78	28	TRS
2	154	0.40	0.74	23	empty

Interfaces

3 interfaces between chains.

B–C · 238 Å² buried · 2 hydrogen bonds · protein-protein
A–C · 177 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 172 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1TTO · Crystal structure of the Rnase T1 variant R2 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P00651
Elsewhere: RCSB PDB 1TTO · PDBe 1TTO · UniProt P00651

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